Abstract
The partial molar volume of lysozyme and bovine serum albumin in aqueous solutions at different pH values and in aqueous solutions containing sodium chloride, ammonium chloride, sodium sulfate, or ammonium sulfate at different concentrations at pH 7.0 was investigated experimentally at 298.15 K and 1 bar. It was found that the influence of the pH value and the salts on the partial molar volume of the proteins is small, but trends were measurable. Furthermore, the partial molar volume of lysozyme in pure water at different pH values and in aqueous solutions with different sodium chloride concentrations at pH 7.0 was predicted by molecular simulations. The predictions are in good agreement with the experimental data.